Acid precipitation and embryonic mortality of spotted salamanders, Ambystoma maculatum

Science ◽  
1976 ◽  
Vol 192 (4234) ◽  
pp. 68-70 ◽  
Author(s):  
F. Pough
1981 ◽  
Vol 59 (7) ◽  
pp. 1339-1343
Author(s):  
Raymond Leclair Jr. ◽  
Jean-Pierre Bourassa

Observations during spring 1980 in two temporary pools near Trois-Rivières, Quebec, and in the laboratory show that Dipterian chironomid larvae can go through the gelatinous envelopes of egg masses of the salamander Ambystoma maculatum and consume developing eggs and embryos. In the clear water pool, egg spawns are heavily infested by the chironomid Parachironomus cf. forceps and embryonic mortality reaches 70 to 100%. In the dark water pool, infestation by an unidentified chironomid is low and embryonic mortality reaches 8%. In both cases, chironomid larvae leave the egg masses some 9 days before hatching of the salamanders. Fortuitous exploitation of a readily available resource is hypothesized; the frequency and precision of the observed phenological coincidence, due to the presence of other syntopic amphibian spring breeders, will be examined further.


1982 ◽  
Vol 16 (3) ◽  
pp. 162-169 ◽  
Author(s):  
Norman R. Glass ◽  
Dean E. Arnold ◽  
James N. Galloway ◽  
George R. Hendrey ◽  
Jeffrey J. Lee ◽  
...  
Keyword(s):  

1964 ◽  
Vol 11 (01) ◽  
pp. 064-074 ◽  
Author(s):  
Robert H Wagner ◽  
William D McLester ◽  
Marion Smith ◽  
K. M Brinkhous

Summary1. The use of several amino acids, glycine, alpha-aminobutyric acid, alanine, beta-alanine, and gamma-aminobutyric acid, as plasma protein precipitants is described.2. A specific procedure is detailed for the preparation of canine antihemophilic factor (AHF, Factor VIII) in which glycine, beta-alanine, and gammaaminobutyric acid serve as the protein precipitants.3. Preliminary results are reported for the precipitation of bovine and human AHF with amino acids.


1972 ◽  
Vol 70 (1) ◽  
pp. 48-55 ◽  
Author(s):  
Mario A. Pisarev ◽  
Noe Altschuler ◽  
Leslie J. DeGroot

ABSTRACT The process of secretion of the thyroid hormone involves several steps: pinocytosis of thyroglobulin, fusion of the colloid droplets with the lysosomes, digestion of thyroglobulin by a cathepsin, dehalogenation of tyrosines and release of thyronines into the blood stream. The present paper describes a double isotope technique for studying the first two steps. Thyrotrophin (TSH) administration to rats increased the radioactivity present in all fractions, specially in the 15 000 × g pellet. When the subcellular distribution of acid phosphatase was determined, the highest specific activity was found in this fraction, thus indicating the presence of lysosomes. The content of radioactive materials in the 15 000 × g pellet was analyzed by trichloroacetic acid precipitation and by ascending paper chromatography using n-butanol:ethanol:ammonium hydroxide (5:1:2;v/v) as solvent system. The results obtained showed that 90% of the radioactivity was protein bound and strongly suggest that this material is thyroglobulin.


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